Computational Investigation of the Initial Two-Electron, Two-Proton Steps in the Reaction Mechanism of Hydroxylamine Oxidoreductase
Author:
Affiliation:
1. Department of Chemistry, Babes-Bolyai University, Cluj-Napoca, RO-400028 Romania
Funder
Ministry of Education and Research, Romanian
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp507023a
Reference33 articles.
1. Hydroxylamine oxidoreductase: a 20-heme, 200,000 molecular weight cytochrome c with unusual denaturation properties which forms a 63,000 molecular weight monomer after heme removal
2. The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
3. Hydroxylamine oxidoreductase from Nitrosomonas europaea is a multimer of an octa-heme subunit
4. Evidence for the structure of the active site heme P460 in hydroxylamine oxidoreductase of Nitrosomonas
5. Principles of structure, bonding, and reactivity for metal nitrosyl complexes
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